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A peptide bond covalently attaches amino acids through a dehydration reaction. One amino acid's carboxyl group and another amino acid's amino group combine, releasing a water molecule. The resulting bond is the peptide bond. The products that such linkages form are peptides. As more amino acids join this growing chain, the resulting chain is a polypeptide. Each polypeptide has a free amino group at one end. This end has the N-terminal, or the amino-terminal, and the other end has a free...
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Cryptides: latent peptides everywhere.

Federica Iavarone1, Claudia Desiderio2, Alberto Vitali2

  • 1a Istituto di Biochimica e Biochimica Clinica, Università Cattolica , Roma , Italy.

Critical Reviews in Biochemistry and Molecular Biology
|March 23, 2018
PubMed
Summary
This summary is machine-generated.

Thousands of protein fragments, called cryptides, have unique functions distinct from their parent proteins. This emerging field investigates these naturally occurring peptides found across kingdoms, with potential applications in medicine.

Keywords:
Cryptidesalbuminencrypted peptideshemoglobinhemorphinshidden peptidesimmunoglobulinslatent peptides

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Area of Science:

  • Proteomics
  • Biochemistry
  • Molecular Biology

Background:

  • Top-down proteomic platforms are identifying numerous naturally occurring protein fragments.
  • While some fragments result from protein degradation, many possess distinct biological functions.
  • These functional fragments, termed cryptides, represent a novel area of scientific inquiry.

Purpose of the Study:

  • To highlight the widespread presence and significance of cryptides.
  • To explore examples of cryptides from common biological sources.
  • To underscore the need for advanced platforms for cryptide discovery and functional screening.

Main Methods:

  • Utilized top-down proteomic analysis to identify naturally occurring protein fragments.
  • Reviewed existing literature to describe well-studied cryptides from various sources.
  • Selected representative examples of cryptides from serum albumin, immunoglobulins, hemoglobin, milk, and saliva proteins.

Main Results:

  • Identified thousands of naturally occurring protein fragments through proteomic surveys.
  • Confirmed the presence of functional cryptides in common biological sources like serum albumin and hemoglobin.
  • Demonstrated that cryptides can have functions unrelated to their parent proteins.

Conclusions:

  • Cryptides are prevalent across animal and plant kingdoms, constituting a significant -omic field.
  • Further development of -omic platforms is crucial for discovering and functionally screening new cryptides.
  • Cryptides hold potential for developing novel peptides and peptidomimetics for diverse applications.